Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows
ABSTRACTA major driver for the recent investment surge in bispecific antibody (bsAb) platforms and products is the multitude of distinct mechanisms of action that bsAbs offer compared to a combination of two monoclonal antibodies. Four bsAb products were granted first regulatory approvals in the US...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2024-12-01
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| Series: | mAbs |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/19420862.2024.2311992 |
| _version_ | 1797300530120228864 |
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| author | Caitlin Fawcett Joseph. R. Tickle Charlotte. H. Coles |
| author_facet | Caitlin Fawcett Joseph. R. Tickle Charlotte. H. Coles |
| author_sort | Caitlin Fawcett |
| collection | DOAJ |
| description | ABSTRACTA major driver for the recent investment surge in bispecific antibody (bsAb) platforms and products is the multitude of distinct mechanisms of action that bsAbs offer compared to a combination of two monoclonal antibodies. Four bsAb products were granted first regulatory approvals in the US or EU during 2023 and the biopharmaceutical industry pipeline is brimming with bsAb candidates across a broad range of therapeutic applications. In previously reported bsAb discovery campaigns, following a hypothesis-based choice of two specific target proteins, selections and screening activities have often been performed in mono-specific formats. The conversion to bispecific modalities has usually been positioned toward the end of the discovery process and has involved small numbers of lead molecules, largely due to challenges in expressing, purifying, and analyzing large numbers of bsAbs. In this review, we discuss emerging strategies to facilitate the production of expanded bsAb panels, focusing particularly upon combinatorial methods to generate bsAb matrices. Such technologies will enable screening in. bispecific formats at earlier stages of discovery campaigns, not only widening the accessible protein space to maximize chances of success, but also advancing empirical bi-target validation activities to assess initial target selection hypotheses. |
| first_indexed | 2024-03-07T23:08:30Z |
| format | Article |
| id | doaj.art-d25e377005614e7786093a9c226c1ac1 |
| institution | Directory Open Access Journal |
| issn | 1942-0862 1942-0870 |
| language | English |
| last_indexed | 2024-03-07T23:08:30Z |
| publishDate | 2024-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | mAbs |
| spelling | doaj.art-d25e377005614e7786093a9c226c1ac12024-02-21T16:40:30ZengTaylor & Francis GroupmAbs1942-08621942-08702024-12-0116110.1080/19420862.2024.2311992Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflowsCaitlin Fawcett0Joseph. R. Tickle1Charlotte. H. Coles2Large Molecule Discovery, GSK, GSK Medicines Research Centre, Stevenage, UKLarge Molecule Discovery, GSK, GSK Medicines Research Centre, Stevenage, UKLarge Molecule Discovery, GSK, GSK Medicines Research Centre, Stevenage, UKABSTRACTA major driver for the recent investment surge in bispecific antibody (bsAb) platforms and products is the multitude of distinct mechanisms of action that bsAbs offer compared to a combination of two monoclonal antibodies. Four bsAb products were granted first regulatory approvals in the US or EU during 2023 and the biopharmaceutical industry pipeline is brimming with bsAb candidates across a broad range of therapeutic applications. In previously reported bsAb discovery campaigns, following a hypothesis-based choice of two specific target proteins, selections and screening activities have often been performed in mono-specific formats. The conversion to bispecific modalities has usually been positioned toward the end of the discovery process and has involved small numbers of lead molecules, largely due to challenges in expressing, purifying, and analyzing large numbers of bsAbs. In this review, we discuss emerging strategies to facilitate the production of expanded bsAb panels, focusing particularly upon combinatorial methods to generate bsAb matrices. Such technologies will enable screening in. bispecific formats at earlier stages of discovery campaigns, not only widening the accessible protein space to maximize chances of success, but also advancing empirical bi-target validation activities to assess initial target selection hypotheses.https://www.tandfonline.com/doi/10.1080/19420862.2024.2311992Antibody engineeringbiopharmaceutical drug discoveryBispecific antibodychemical conjugationmass spectrometry |
| spellingShingle | Caitlin Fawcett Joseph. R. Tickle Charlotte. H. Coles Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows mAbs Antibody engineering biopharmaceutical drug discovery Bispecific antibody chemical conjugation mass spectrometry |
| title | Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows |
| title_full | Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows |
| title_fullStr | Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows |
| title_full_unstemmed | Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows |
| title_short | Facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows |
| title_sort | facilitating high throughput bispecific antibody production and potential applications within biopharmaceutical discovery workflows |
| topic | Antibody engineering biopharmaceutical drug discovery Bispecific antibody chemical conjugation mass spectrometry |
| url | https://www.tandfonline.com/doi/10.1080/19420862.2024.2311992 |
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